Bionic-immobilized recombinant lipase obtained via bio-silicification and its catalytic performance in biodiesel production. (15th November 2021)
- Record Type:
- Journal Article
- Title:
- Bionic-immobilized recombinant lipase obtained via bio-silicification and its catalytic performance in biodiesel production. (15th November 2021)
- Main Title:
- Bionic-immobilized recombinant lipase obtained via bio-silicification and its catalytic performance in biodiesel production
- Authors:
- Zhang, Jun
Chen, Xiaoyan
Lv, Pengmei
Luo, Wen
Wang, Zhiyuan
Xu, Jingliang
Wang, Zhongming - Abstract:
- Graphical abstract: Highlights: Recombinant lipase with histidine tag was bionic-immobilized via bio-silicification. The bionic-immobilization efficiency was 97.71%; the activity recovery was 89.62%. The immobilization mechanism was illustrated via molecular dynamics simulation. The bionic-immobilized lipase exhibited excellent thermal and storage stability. The immobilized lipase showed a biodiesel yield of 91.04% within 12 h and 45 °C. Abstract: In this study, bio-silicification was employed to develop a green and simple bionic-immobilization method for the immobilization of recombinant lipase. The results showed that under the optimized bionic-immobilization conditions, a maximum immobilization efficiency and an activity recovery of 97.71% and 89.62%, respectively, were obtained. Further, bionic-immobilization significantly improved the thermal stability, storage stability, and short-chain alcohol resistance of the bionic-immobilized lipase. Furthermore, molecular dynamics simulation of the bionic-immobilization mechanism revealed that the key amino acid residues that facilitated the binding of the recombinant lipase to silica particles included Arg336, Lys345, His391, His392, His394, and His395, indicating that hydrogen bonds had a special effect in intermolecular recognition, and the active center of the bionic-immobilized lipase favored substrate entry due to the conformational changes of Phe291 and Ile320. Finally, biodiesel was prepared using the bionic-immobilizedGraphical abstract: Highlights: Recombinant lipase with histidine tag was bionic-immobilized via bio-silicification. The bionic-immobilization efficiency was 97.71%; the activity recovery was 89.62%. The immobilization mechanism was illustrated via molecular dynamics simulation. The bionic-immobilized lipase exhibited excellent thermal and storage stability. The immobilized lipase showed a biodiesel yield of 91.04% within 12 h and 45 °C. Abstract: In this study, bio-silicification was employed to develop a green and simple bionic-immobilization method for the immobilization of recombinant lipase. The results showed that under the optimized bionic-immobilization conditions, a maximum immobilization efficiency and an activity recovery of 97.71% and 89.62%, respectively, were obtained. Further, bionic-immobilization significantly improved the thermal stability, storage stability, and short-chain alcohol resistance of the bionic-immobilized lipase. Furthermore, molecular dynamics simulation of the bionic-immobilization mechanism revealed that the key amino acid residues that facilitated the binding of the recombinant lipase to silica particles included Arg336, Lys345, His391, His392, His394, and His395, indicating that hydrogen bonds had a special effect in intermolecular recognition, and the active center of the bionic-immobilized lipase favored substrate entry due to the conformational changes of Phe291 and Ile320. Finally, biodiesel was prepared using the bionic-immobilized lipase as catalyst, and after optimizing the enzymatic process, the biodiesel yield reached 91.04% using 20% immobilized lipase dosage within 12 h at 45 °C, and a catalytic activity of 55.02% was observed following the reutilization of the bionic-immobilized lipase seven times. These findings suggest that bionic-immobilization is a novel and rapid method to realize recombinant enzyme immobilization, and can provide economic and ecological support for the biocatalytic preparation of industrial products. … (more)
- Is Part Of:
- Fuel. Volume 304(2021)
- Journal:
- Fuel
- Issue:
- Volume 304(2021)
- Issue Display:
- Volume 304, Issue 2021 (2021)
- Year:
- 2021
- Volume:
- 304
- Issue:
- 2021
- Issue Sort Value:
- 2021-0304-2021-0000
- Page Start:
- Page End:
- Publication Date:
- 2021-11-15
- Subjects:
- Lipase -- Bionic-immobilization -- Biodiesel -- Bio-silicification -- Molecular dynamics simulation
Fuel -- Periodicals
Coal -- Periodicals
Coal
Fuel
Periodicals
662.6 - Journal URLs:
- http://www.sciencedirect.com/science/journal/latest/00162361 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.fuel.2021.121594 ↗
- Languages:
- English
- ISSNs:
- 0016-2361
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 4048.000000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 19588.xml